Reviewed, UniProtKB/Swiss-Prot P31318 (ARG56_SCHPO)

Names and origin

Protein names

Recommended name:
    Protein arg11, mitochondrial
Cleaved into the following 2 chains:
    1- Recommended name:
            N-acetyl-gamma-glutamyl-phosphate reductase
              EC=1.2.1.38
        Alternative name(s):
            N-acetyl-glutamate semialdehyde dehydrogenase
              Short name=NAGSA dehydrogenase
    2- Recommended name:
            Acetylglutamate kinase
              EC=2.7.2.8
        Alternative name(s):
            NAG kinase
              Short name=AGK
            N-acetyl-L-glutamate 5-phosphotransferase

Gene names

Name:	arg11
ORF Names:	SPAC4G9.09c

Organism

Schizosaccharomyces pombe (Fission yeast) [Complete proteome]

Taxonomic identifier

4896 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length	885 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Catalytic activity	N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate = N-acetyl-5-glutamyl phosphate + NADPH. ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamate 5-phosphate.
Enzyme regulation	The kinase activity is inhibited by arginine.
Pathway	Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4. Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 3/4.
Subcellular location	Mitochondrion.
Post-translational modification	The protein precursor is cleaved into the two biologically active enzymes, the kinase and the reductase.
Sequence similarities	In the N-terminal section; belongs to the acetylglutamate kinase family. In the C-terminal section; belongs to the NAGSA dehydrogenase family.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Arginine biosynthesis
Cellular component	Mitochondrion
Domain	Transit peptide
Ligand	ATP-binding NADP Nucleotide-binding
Molecular function	Kinase Oxidoreductase Transferase
PTM	Cleavage on pair of basic residues
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	arginine biosynthetic process Ref.1 Inferred from genetic interaction. Source: GeneDB_SPombe oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	mitochondrial matrix Ref.1 Inferred from direct assay. Source: GeneDB_SPombe
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW N-acetyl-gamma-glutamyl-phosphate reductase activity Ref.1 Inferred from genetic interaction. Source: GeneDB_SPombe NAD or NADH binding Inferred from electronic annotation. Source: InterPro acetylglutamate kinase activity Ref.1 Inferred from genetic interaction. Source: GeneDB_SPombe protein dimerization activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 59	59	Mitochondrion Potential
	Chain	60 – 550	491	Acetylglutamate kinase Potential		PRO_0000002071
	Chain	551 – 885	335	N-acetyl-gamma-glutamyl-phosphate reductase Potential		PRO_0000002072
Sites
	Active site	703	1	By similarity
Natural variations
	Natural variant	261	1	V → D in strain: 975.
	Natural variant	345	1	G → P in strain: 975.

Sequences

	Sequence		Length	Mass (Da)
	P31318-1 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 3AA1A5082431B118	FASTA	885	97,705
	10 20 30 40 50 60 MLIELQQIVK SGLVRNGAKH CTKRSLLCSN ASVIASKRFQ GSFAPGQQQP LNPLAKPIEQ 70 80 90 100 110 120 DRDAIIRILS SIGSRREVEQ YLRYFTSFEA QRFAIIKVGG AIITDELDTL AQSLAFLNHV 130 140 150 160 170 180 GLYPIVVHGA GPQLNKILAS RNVEPEYSDG IRITDAETLS VARKVFLEEN AKLVDALEKL 190 200 210 220 230 240 GTRARPITGG VFQAEYLDKE KYKYVGKIVK VNKAPIEHSI RAGTLPILTS MAETASGQLL 250 260 270 280 290 300 NVNADITAGE LARVLKPLKV VYLNEKGGLI NGETKKKISS IYLDREYDGL MKQPWVKYGT 310 320 330 340 350 360 KLKIKEIKEL LDTLPRTSSV AIISTKDLQK ELFTESGAGT LISRGFVINK HDSLDSIPDA 370 380 390 400 410 420 ALENLIIQKN SLAAPSESLK QFKDTLKDRK LRIYSDSFNE SVAIVDTTDS SLPVLLAFGA 430 440 450 460 470 480 ADNNWLNNVV DSILTTLKAD FPSLLWRLQP SAKNLEWFFS KSEGTLFANN FYYFWYGVKD 490 500 510 520 530 540 LNKISKFIQS DKPFADAIIQ TQSTKPPTAS STTNNPSSSQ INQKRSYSTS SLFSKNKKMN 550 560 570 580 590 600 RSLFLKGGKR FFSAEAQKTQ KPLKAVSSKP AKVVLLGARG YTGKNLIGLI NTHPYLELSH 610 620 630 640 650 660 VSSRELEGTK LPGYTKKEIQ YVNLSTDDVK KLEEEGAVDA WVMALPNGVC KPYVDALTSA 670 680 690 700 710 720 NGKSVIVDLS ADYRFEPSWQ YGLPELNDRE ALRNSKRISN PGCYATGSQV GLTPILSLID 730 740 750 760 770 780 GQPSIFGVSG YSGAGTKPSP KNDLNVLTNN LIPYSLTDHI HEREISYRLK QPVAFIPHVA 790 800 810 820 830 840 QWFQGITLTI NVPLKKSITS RELRNLYQDR YNGEPLIHVQ GDVPLVKDNA HKHHVSVGGF 850 860 870 880 GVHSSGKRAV IVVTIDNLLK GAATQALQNL NLSCGYDEYA GIHLD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequencing of arg3 and arg11 genes of Schizosaccharomyces pombe on a 10-kb DNA fragment. Heterologous expression and mitochondrial targeting of their translation products." van Huffel C., Dubois E., Messenguy F. Eur. J. Biochem. 205:33-43(1992) [PubMed: 1313366] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 38365 / 975.
[2]	"The genome sequence of Schizosaccharomyces pombe." Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P. Nature 415:871-880(2002) [PubMed: 11859360] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 38366 / 972.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X63576 Genomic DNA. Translation: CAA45132.1. CU329670 Genomic DNA. Translation: CAA93559.1.
PIR	S22389.
RefSeq	NP_593691.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	2543391.
KEGG	spo:SPAC4G9.09c.
NMPDR	fig|4896.1.peg.3661.
Organism-specific databases
GeneDB_Spombe	SPAC4G9.09c.
Phylogenomic databases
OMA	P31318. WVMALPN.
Enzyme and pathway databases
BioCyc	SPOM-XXX-01:SPOM-XXX-01-001357-MON.
BRENDA	1.2.1.38. 653. 2.7.2.8. 653.
Gene expression databases
ArrayExpress	P31318.
Family and domain databases
InterPro	IPR004662. AcgluKinase. IPR000706. AGPR_act_site. IPR001048. Asp/Glu/Uridylate_kinase. IPR006855. DUF619. IPR011241. NAGK_NAGSA. IPR000534. Semialdehyde_DH_NAD-bd. IPR012280. Semialdhyde_DH_C. [Graphical view]
Gene3D	G3DSA:3.40.1160.10. Aa_kinase. 1 hit.
Pfam	PF00696. AA_kinase. 1 hit. PF04768. DUF619. 1 hit. PF01118. Semialdhyde_dh. 1 hit. PF02774. Semialdhyde_dhC. 1 hit. [Graphical view]
PIRSF	PIRSF036440. ARG5-6. 1 hit.
ProDom	PD003765. AGPR_act_site. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00761. argB. 1 hit. TIGR01850. argC. 1 hit.
PROSITE	PS01224. ARGC. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ARG56_SCHPO

Accession

Primary (citable) accession number: P31318

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 79 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)